node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
aadK | blt | BSU26790 | BSU26590 | Aminoglycoside 6-adenylyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; To E.faecalis AadE. | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | 0.733 |
blt | aadK | BSU26590 | BSU26790 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Aminoglycoside 6-adenylyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; To E.faecalis AadE. | 0.733 |
blt | bltD | BSU26590 | BSU26600 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Spermine/spermidine acetyltransferase; Acetylates both spermidine and spermine at primary propyl amine moieties, with spermine being the preferred substrate. | 0.946 |
blt | bmrA | BSU26590 | BSU34820 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | 0.917 |
blt | bmrR | BSU26590 | BSU24020 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Transcriptional regulator (MerR family); Activates transcription of the bmr gene in response to structurally dissimilar drugs. Binds rhodamine as an inducer. | 0.767 |
blt | lmrB | BSU26590 | BSU02670 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Efflux transporter; Proton-dependent transporter. May mediate the efflux of lincomycin; Belongs to the major facilitator superfamily. EmrB family. | 0.751 |
blt | mdr | BSU26590 | BSU03070 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | 0.938 |
blt | ydfK | BSU26590 | BSU05450 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.926 |
blt | yjbB | BSU26590 | BSU11480 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Putative exporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.848 |
blt | yttB | BSU26590 | BSU30350 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.681 |
blt | yxaM | BSU26590 | BSU39930 | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | Putative efflux transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.848 |
bltD | blt | BSU26600 | BSU26590 | Spermine/spermidine acetyltransferase; Acetylates both spermidine and spermine at primary propyl amine moieties, with spermine being the preferred substrate. | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | 0.946 |
bmrA | blt | BSU34820 | BSU26590 | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | 0.917 |
bmrA | mdr | BSU34820 | BSU03070 | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | 0.850 |
bmrR | blt | BSU24020 | BSU26590 | Transcriptional regulator (MerR family); Activates transcription of the bmr gene in response to structurally dissimilar drugs. Binds rhodamine as an inducer. | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | 0.767 |
bmrR | ydfK | BSU24020 | BSU05450 | Transcriptional regulator (MerR family); Activates transcription of the bmr gene in response to structurally dissimilar drugs. Binds rhodamine as an inducer. | Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. | 0.867 |
lmrB | blt | BSU02670 | BSU26590 | Efflux transporter; Proton-dependent transporter. May mediate the efflux of lincomycin; Belongs to the major facilitator superfamily. EmrB family. | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | 0.751 |
lmrB | mdr | BSU02670 | BSU03070 | Efflux transporter; Proton-dependent transporter. May mediate the efflux of lincomycin; Belongs to the major facilitator superfamily. EmrB family. | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | 0.438 |
mdr | blt | BSU03070 | BSU26590 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family. | 0.938 |
mdr | bmrA | BSU03070 | BSU34820 | Multidrug-efflux transporter; Confers resistance to puromycin, tosufloxacin and norfloxacin. | Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). | 0.850 |